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lüll Solid-state NMR studies of amyloid fibril structure Tycko RAnnu Rev Phys Chem 2011[]; 62 (ä): 279-99Current interest in amyloid fibrils stems from their involvement in neurodegenerative and other diseases and from their role as an alternative structural state for many peptides and proteins. Solid-state nuclear magnetic resonance (NMR) methods have the unique capability of providing detailed structural constraints for amyloid fibrils, sufficient for the development of full molecular models. In this article, recent progress in the application of solid-state NMR to fibrils associated with Alzheimer's disease, prion fibrils, and related systems is reviewed, along with relevant developments in solid-state NMR techniques and technology.|*Models, Molecular[MESH]|Alzheimer Disease/metabolism[MESH]|Amyloid/*chemistry/metabolism/*ultrastructure[MESH]|Humans[MESH]|Magnetic Resonance Imaging/methods[MESH]|Magnetic Resonance Spectroscopy/*methods[MESH]|Microscopy, Electron, Transmission/methods[MESH]|Peptide Fragments/chemistry/metabolism[MESH]|Prions/chemistry/metabolism[MESH]|Protein Conformation[MESH]|Protein Structure, Secondary[MESH]|Proteins/chemistry/metabolism[MESH] |